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Conserved domains on  [gi|690619407|gb|AIQ20620|]
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hypothetical protein H70357_30950 [Paenibacillus sp. FSL H7-0357]

Protein Classification

macro domain-containing protein( domain architecture ID 10121048)

macro domain-containing protein functions in the recognition, interpretation, and turnover of ADP-ribose (ADPr) signaling, such as ADP-ribose 1''-phosphate phosphatase that is involved in the metabolism of ADP-ribose 1''-phosphate (Appr1p) which is produced as a consequence of tRNA splicing

CATH:  3.40.220.10
Gene Ontology:  GO:0072570
PubMed:  15902274|26844395
SCOP:  4000521

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Macro_Poa1p-like cd02901
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ...
 2-131 3.55e-46

macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this family show similarity to the yeast protein Poa1p, reported to be a phosphatase specific for Appr-1"-p, a tRNA splicing metabolite. Poa1p may play a role in tRNA splicing regulation.


:

Pssm-ID: 394873  Cd Length: 135  Bit Score: 146.24  E-value: 3.55e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690619407   2 EFQEIKKDLFSMPEDYCLAHCISADAKMGAGIAVQFRKRFKLSSLQEKANRNELLvGECYKVER------VFNLITKSKY 75
Cdd:cd02901    1 KITYVKGDLFACPETKSLAHCCNCDGVMGKGIALQFKKKPGRVEELRAQCKKKLL-GGVAVLKRdgvkryIYYLITKKSY 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 690619407  76 WQKPTYDTLTLSLRAMKEICLQEAVNQIAMPEIGCGLDKLQWEKVKEIIMKEFKDT 131
Cdd:cd02901   80 GPKPTYEALRSSLEELREHCRENGVTSVAMPRIGCGLDGLDWEEVEPILKEVFDDR 135
 
Name Accession Description Interval E-value
Macro_Poa1p-like cd02901
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ...
 2-131 3.55e-46

macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this family show similarity to the yeast protein Poa1p, reported to be a phosphatase specific for Appr-1"-p, a tRNA splicing metabolite. Poa1p may play a role in tRNA splicing regulation.


Pssm-ID: 394873  Cd Length: 135  Bit Score: 146.24  E-value: 3.55e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690619407   2 EFQEIKKDLFSMPEDYCLAHCISADAKMGAGIAVQFRKRFKLSSLQEKANRNELLvGECYKVER------VFNLITKSKY 75
Cdd:cd02901    1 KITYVKGDLFACPETKSLAHCCNCDGVMGKGIALQFKKKPGRVEELRAQCKKKLL-GGVAVLKRdgvkryIYYLITKKSY 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 690619407  76 WQKPTYDTLTLSLRAMKEICLQEAVNQIAMPEIGCGLDKLQWEKVKEIIMKEFKDT 131
Cdd:cd02901   80 GPKPTYEALRSSLEELREHCRENGVTSVAMPRIGCGLDGLDWEEVEPILKEVFDDR 135
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 29-130 1.28e-09

O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441713  Cd Length: 168  Bit Score: 53.26  E-value: 1.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690619407  29 MGAGIAVQFRKRFK---LSSLQEKANRNELLVGECY-------KVERVFNLITKskYWQ---KPTYDTLTLSLRAMKEIC 95
Cdd:COG2110   26 GGGGVAGAIHRAAGpelLEECRRLCKQGGCPTGEAVitpagnlPAKYVIHTVGP--VWRgggPSEEELLASCYRNSLELA 103

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 690619407  96 LQEAVNQIAMPEIGCGLDKLQWEKVKEIIMKEFKD 130
Cdd:COG2110  104 EELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRD 138
tk.4 PHA02595
hypothetical protein; Provisional
 1-137 1.58e-09

hypothetical protein; Provisional


Pssm-ID: 222899  Cd Length: 154  Bit Score: 52.77  E-value: 1.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690619407   1 MEFQEIKKDLFSM--PEDYCLAHCISADAKMGAGIAVQFRKRF----KLSSLQEKANRNELLVGECY------KVERVFN 68
Cdd:PHA02595   1 MIVDYIKGDIVALflQGKGNIAHGCNCFHTMGSGIAGQLAKAFpqilEADKLTTEGDVEKLGTFSVWekyvggHKAYCFN 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690619407  69 LITKSKYWQKPTYDTLTLSLRAMKEICLQEAVNQ-IAMPEIGCGLDKLQWEKVKEIIMKEFKDtpIQITV 137
Cdd:PHA02595  81 LYTQFDPGPNLEYSALMNCFEELNEVFEGTLFKPtIYIPRIGAGIAGGDWDKIEAIIDEATPD--IDIVV 148
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 2-124 2.96e-09

Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by reciprocal PSI-BLAST searches (unpublished results, and Pehrson _ Fuji).


Pssm-ID: 214701  Cd Length: 133  Bit Score: 51.54  E-value: 2.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690619407     2 EFQEIKKDLFSMPEDyCLAHCISADAKMGAGIAVQFRKRFKLSSLQE---KANRNELLVGECYKVE-------RVFNLIT 71
Cdd:smart00506   1 ILKVVKGDITKPRAD-AIVNAANSDGAHGGGVAGAIARAAGKALSKEevrKLAGGECPVGTAVVTEggnlpakYVIHAVG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 690619407    72 K--SKYWQKPtYDTLTLSLRAMKEICLQEAVNQIAMPEIGCGLDKLQWEKVKEII 124
Cdd:smart00506  80 PraSGHSKEG-FELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKDRSAQAL 133
 
Name Accession Description Interval E-value
Macro_Poa1p-like cd02901
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ...
 2-131 3.55e-46

macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this family show similarity to the yeast protein Poa1p, reported to be a phosphatase specific for Appr-1"-p, a tRNA splicing metabolite. Poa1p may play a role in tRNA splicing regulation.


Pssm-ID: 394873  Cd Length: 135  Bit Score: 146.24  E-value: 3.55e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690619407   2 EFQEIKKDLFSMPEDYCLAHCISADAKMGAGIAVQFRKRFKLSSLQEKANRNELLvGECYKVER------VFNLITKSKY 75
Cdd:cd02901    1 KITYVKGDLFACPETKSLAHCCNCDGVMGKGIALQFKKKPGRVEELRAQCKKKLL-GGVAVLKRdgvkryIYYLITKKSY 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 690619407  76 WQKPTYDTLTLSLRAMKEICLQEAVNQIAMPEIGCGLDKLQWEKVKEIIMKEFKDT 131
Cdd:cd02901   80 GPKPTYEALRSSLEELREHCRENGVTSVAMPRIGCGLDGLDWEEVEPILKEVFDDR 135
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 19-127 4.92e-12

macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Macrodomains include the yeast macrodomain Poa1 which is a phosphatase of ADP-ribose-1"-phosphate, a by-product of tRNA splicing. Some macrodomains have ADPr-unrelated binding partners such as the coronavirus SUD-N (N-terminal subdomain) and SUD-M (middle subdomain) of the SARS-unique domain (SUD) which bind G-quadruplexes (unusual nucleic-acid structures formed by consecutive guanosine nucleotides). Macrodomains regulate a wide variety of cellular and organismal processes, including DNA damage repair, signal transduction, and immune response.


Pssm-ID: 394871  Cd Length: 121  Bit Score: 58.56  E-value: 4.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690619407  19 LAHCISADAKMGAGIAVQFRKRFKLSslQEKANRNELLVGECYKVE------------RVFNLITKSKYWQKPTYDTLTL 86
Cdd:cd02749    3 IVNPANNDLYLGGGVAKAISKKAGGD--LQEECEERKKNGYLKVGEvavtkggnlparYIIHVVGPVASSKKKTYEPLKK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 690619407  87 SLRAMKEICLQEAVNQIAMPEIGCGLDKLQWEKVKEIIMKE 127
Cdd:cd02749   81 CVKNCLSLADEKGLKSVAFPAIGTGIAGFPPEEAARIMLEA 121
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 29-130 1.28e-09

O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441713  Cd Length: 168  Bit Score: 53.26  E-value: 1.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690619407  29 MGAGIAVQFRKRFK---LSSLQEKANRNELLVGECY-------KVERVFNLITKskYWQ---KPTYDTLTLSLRAMKEIC 95
Cdd:COG2110   26 GGGGVAGAIHRAAGpelLEECRRLCKQGGCPTGEAVitpagnlPAKYVIHTVGP--VWRgggPSEEELLASCYRNSLELA 103

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 690619407  96 LQEAVNQIAMPEIGCGLDKLQWEKVKEIIMKEFKD 130
Cdd:COG2110  104 EELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRD 138
tk.4 PHA02595
hypothetical protein; Provisional
 1-137 1.58e-09

hypothetical protein; Provisional


Pssm-ID: 222899  Cd Length: 154  Bit Score: 52.77  E-value: 1.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690619407   1 MEFQEIKKDLFSM--PEDYCLAHCISADAKMGAGIAVQFRKRF----KLSSLQEKANRNELLVGECY------KVERVFN 68
Cdd:PHA02595   1 MIVDYIKGDIVALflQGKGNIAHGCNCFHTMGSGIAGQLAKAFpqilEADKLTTEGDVEKLGTFSVWekyvggHKAYCFN 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690619407  69 LITKSKYWQKPTYDTLTLSLRAMKEICLQEAVNQ-IAMPEIGCGLDKLQWEKVKEIIMKEFKDtpIQITV 137
Cdd:PHA02595  81 LYTQFDPGPNLEYSALMNCFEELNEVFEGTLFKPtIYIPRIGAGIAGGDWDKIEAIIDEATPD--IDIVV 148
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 2-124 2.96e-09

Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by reciprocal PSI-BLAST searches (unpublished results, and Pehrson _ Fuji).


Pssm-ID: 214701  Cd Length: 133  Bit Score: 51.54  E-value: 2.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690619407     2 EFQEIKKDLFSMPEDyCLAHCISADAKMGAGIAVQFRKRFKLSSLQE---KANRNELLVGECYKVE-------RVFNLIT 71
Cdd:smart00506   1 ILKVVKGDITKPRAD-AIVNAANSDGAHGGGVAGAIARAAGKALSKEevrKLAGGECPVGTAVVTEggnlpakYVIHAVG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 690619407    72 K--SKYWQKPtYDTLTLSLRAMKEICLQEAVNQIAMPEIGCGLDKLQWEKVKEII 124
Cdd:smart00506  80 PraSGHSKEG-FELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKDRSAQAL 133
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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